LEA proteins: IDPs with versatile functions in cellular dehydration tolerance

2012 ◽  
Vol 40 (5) ◽  
pp. 1000-1003 ◽  
Author(s):  
Dirk K. Hincha ◽  
Anja Thalhammer
Keyword(s):  
Late Embryogenesis Abundant ◽  
Plant Tissues ◽  
Lea Proteins ◽  
Plant Seed ◽  
Dehydration Tolerance ◽  
Intrinsically Disordered ◽  
Cellular Dehydration ◽  
Late Embryogenesis ◽  
Micro Organisms ◽  
Physiological And Biochemical

LEA (late embryogenesis abundant) proteins were originally described almost 30 years ago as accumulating late in plant seed development. They were later found to be induced in vegetative plant tissues under environmental stress conditions and also in desiccation-tolerant micro-organisms and invertebrates. Although they are widely assumed to play crucial roles in cellular dehydration tolerance, their physiological and biochemical functions are largely unknown. Most LEA proteins are predicted to be intrinsically disordered and this has been experimentally verified in several cases. In addition, some LEA proteins partially fold, mainly into α-helices, during drying or in the presence of membranes. Recent studies have concentrated on the potential roles of LEA proteins in stabilizing membranes or sensitive enzymes during freezing or drying, and the present review concentrates on these two possible functions of LEA proteins in cellular dehydration tolerance.

scholarly journals Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4930 ◽  
Author(s):  
Leidys French-Pacheco ◽  
Cesar L. Cuevas-Velazquez ◽  
Lina Rivillas-Acevedo ◽  
Alejandra A. Covarrubias ◽  
Carlos Amero
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Intrinsically Disordered Protein ◽  
Late Embryogenesis Abundant ◽  
Terminal Region ◽  
Late Embryogenesis Abundant Protein ◽  
Lea Proteins ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Late Embryogenesis

Late embryogenesis abundant (LEA) proteins accumulate in plants during adverse conditions and their main attributed function is to confer tolerance to stress. One of the deleterious effects of the adverse environment is the accumulation of metal ions to levels that generate reactive oxygen species, compromising the survival of cells. AtLEA4-5, a member of group 4 of LEAs in Arabidopsis, is an intrinsically disordered protein. It has been shown that their N-terminal region is able to undergo transitions to partially folded states and prevent the inactivation of enzymes. We have characterized metal ion binding to AtLEA4-5 by circular dichroism, electronic absorbance spectroscopy (UV–vis), electron paramagnetic resonance, dynamic light scattering, and isothermal titration calorimetry. The data shows that AtLEA4-5 contains a single binding site for Ni(II), while Zn(II) and Cu(II) have multiple binding sites and promote oligomerization. The Cu(II) interacts preferentially with histidine residues mostly located in the C-terminal region with moderate affinity and different coordination modes. These results and the lack of a stable secondary structure formation indicate that an ensemble of conformations remains accessible to the metal for binding, suggesting the formation of a fuzzy complex. Our results support the multifunctionality of LEA proteins and suggest that the C-terminal region of AtLEA4-5 could be responsible for antioxidant activity, scavenging metal ions under stress conditions while the N-terminal could function as a chaperone.

scholarly journals Characterization of the Heat-Stable Proteome During Seed Germination in Arabidopsis with Special Focus on LEA Proteins

2021 ◽  
Vol 22 (15) ◽  
pp. 8172
Author(s):  
Orarat Ginsawaeng ◽  
Michal Gorka ◽  
Alexander Erban ◽  
Carolin Heise ◽  
Franziska Brueckner ◽  
...  
Keyword(s):  
Seed Germination ◽  
Seedling Establishment ◽  
Intrinsically Disordered Proteins ◽  
Late Embryogenesis Abundant ◽  
Disordered Proteins ◽  
Similar Proportion ◽  
Special Focus ◽  
Lea Proteins ◽  
Intrinsically Disordered ◽  
Heat Stable

During seed germination, desiccation tolerance is lost in the radicle with progressing radicle protrusion and seedling establishment. This process is accompanied by comprehensive changes in the metabolome and proteome. Germination of Arabidopsis seeds was investigated over 72 h with special focus on the heat-stable proteome including late embryogenesis abundant (LEA) proteins together with changes in primary metabolites. Six metabolites in dry seeds known to be important for seed longevity decreased during germination and seedling establishment, while all other metabolites increased simultaneously with activation of growth and development. Thermo-stable proteins were associated with a multitude of biological processes. In the heat-stable proteome, a relatively similar proportion of fully ordered and fully intrinsically disordered proteins (IDP) was discovered. Highly disordered proteins were found to be associated with functional categories development, protein, RNA and stress. As expected, the majority of LEA proteins decreased during germination and seedling establishment. However, four germination-specific dehydrins were identified, not present in dry seeds. A network analysis of proteins, metabolites and amino acids generated during the course of germination revealed a highly connected LEA protein network.

scholarly journals Study of model systems to test the potential function of Artemia group 1 late embryogenesis abundant (LEA) proteins

2015 ◽  
Vol 21 (1) ◽  
pp. 139-154 ◽  
Author(s):  
Alden H. Warner ◽  
Zhi-hao Guo ◽  
Sandra Moshi ◽  
John W. Hudson ◽  
Anna Kozarova
Keyword(s):  
Potential Function ◽  
Late Embryogenesis Abundant ◽  
Model Systems ◽  
Lea Proteins ◽  
Late Embryogenesis ◽  
Group 1

scholarly journals Genome-Wide Identification and Expression Profiles of Late Embryogenesis-Abundant (LEA) Genes during Grain Maturation in Wheat (Triticum aestivum L.)

Genes ◽  
2019 ◽  
Vol 10 (9) ◽  
pp. 696
Author(s):  
Datong Liu ◽  
Jing Sun ◽  
Dongmei Zhu ◽  
Guofeng Lyu ◽  
Chunmei Zhang ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Expression Profiles ◽  
Triticum Aestivum L ◽  
Late Embryogenesis Abundant ◽  
Wheat Breeding ◽  
Pcr Analysis ◽  
Lea Genes ◽  
Cellular Dehydration ◽  
Genome Wide ◽  
Late Embryogenesis

Late embryogenesis-abundant (LEA) genes play important roles in plant growth and development, especially the cellular dehydration tolerance during seed maturation. In order to comprehensively understand the roles of LEA family members in wheat, we carried out a series of analyses based on the latest genome sequence of the bread wheat Chinese Spring. 121 Triticum aestivum L. LEA (TaLEA) genes, classified as 8 groups, were identified and characterized. TaLEA genes are distributed in all chromosomes, most of them with a low number of introns (≤3). Expression profiles showed that most TaLEA genes expressed specifically in grains. By qRT-PCR analysis, we confirmed that 12 genes among them showed high expression levels during late stage grain maturation in two spring wheat cultivars, Yangmai16 and Yangmai15. For most genes, the peak of expression appeared earlier in Yangmai16. Statistical analysis indicated that expression level of 8 genes in Yangmai 16 were significantly higher than Yangmai 15 at 25 days after anthesis. Taken together, our results provide more knowledge for future functional analysis and potential utilization of TaLEA genes in wheat breeding.

‘Dehydrin-like’ proteins and desiccation tolerance in seeds

1994 ◽  
Vol 4 (2) ◽  
pp. 135-141 ◽  
Author(s):  
O. H. Gee ◽  
R. J. Probert ◽  
S. A. Coomber
Keyword(s):  
Desiccation Tolerance ◽  
Consensus Sequence ◽  
Causal Link ◽  
Late Embryogenesis Abundant ◽  
Acer Pseudoplatanus ◽  
Lea Proteins ◽  
Late Embryogenesis ◽  
Group 2 ◽  
Plant Families ◽  
The Relationship

AbstractThe relationship between tolerance of seeds to extreme desiccation and the presence of ‘dehydrinlike’ proteins was investigated in groups of related taxa from the unrelated plant families Aceraceae and Gramineae. Dehydrin-like proteins were identified by Western blot analysis using an antibody raised against a synthetic oligopeptide representing the 23-amino acid consensus sequence common to all group 2 late-embryogenesis-abundant (LEA) proteins.Evidence is presented that seeds of Acer pseudoplatanus and A. saccharinum are desiccation intolerant (recalcitrant) whereas seeds of A. platanoides and A. rubrum are desiccation tolerant (orthodox). Despite these differences, dehydrinlike proteins at 60 and 20 kDa were detected in all four species.Dehydrins at 20 kDa were also detected in seed samples of two aquatic grasses, Porteresia coarctata and Oryza sativa from the tribe Oryzeae, despite seeds of the former rapidly losing viability on drying, whereas O. sativa is one of the best-known examples of desiccation-tolerant seeds. In O. sativa, there was a correlation between contents of dehydrins detected and the proportion of individuals capable of withstanding extreme drying. However, the possibility of a causal link between these parameters is equivocal. Dehydrin-like proteins were also detected in desiccation-sensitive seeds of Zizania palustris, Z. latifolia and Z. texana and desiccation-intolerant seeds of Spartina anglica, all from the Gramineae.The presence of group 2 LEAs is clearly not diagnostic of desiccation tolerance in seeds. However, a more direct correlation with the expression of other groups of LEAs cannot be discounted.

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